Cargando…
Sialylation of EGFR by ST6GAL1 induces receptor activation and modulates trafficking dynamics
Aberrant glycosylation is a hallmark of a cancer cell. One prevalent alteration is an enrichment in α2,6-linked sialylation of N-glycosylated proteins, a modification directed by the ST6GAL1 sialyltransferase. ST6GAL1 is upregulated in many malignancies including ovarian cancer. Prior studies have s...
Autores principales: | Ankenbauer, Katherine E., Rao, Tejeshwar C., Mattheyses, Alexa L., Bellis, Susan L. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cold Spring Harbor Laboratory
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10312608/ https://www.ncbi.nlm.nih.gov/pubmed/37398202 http://dx.doi.org/10.1101/2023.06.03.543566 |
Ejemplares similares
-
Sialylation of EGFR by ST6GAL1 induces receptor activation and modulates trafficking dynamics
por: Ankenbauer, Katherine E., et al.
Publicado: (2023) -
ST6Gal-I–mediated sialylation of the epidermal growth factor receptor modulates cell mechanics and enhances invasion
por: Rao, Tejeshwar C., et al.
Publicado: (2022) -
Regulation of inflammatory signaling by the ST6Gal-I sialyltransferase
por: Holdbrooks, Andrew T., et al.
Publicado: (2020) -
Sialylation of EGFR by the ST6Gal-I sialyltransferase promotes EGFR activation and resistance to gefitinib-mediated cell death
por: Britain, Colleen M., et al.
Publicado: (2018) -
Sox2 promotes expression of the ST6Gal-I glycosyltransferase in ovarian cancer cells
por: Dorsett, Kaitlyn A., et al.
Publicado: (2019)